The only human cathelicidin antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi.
Peptigrity tracks LL-37 across 219 shops with 20 independent lab tests and an average HPLC purity of 99.58%.
LL-37 is a 37-amino-acid amphipathic α-helical peptide — the only human cathelicidin — cleaved from its precursor hCAP-18 by proteinase 3 in neutrophils, macrophages, and epithelial cells at sites of infection or tissue injury. The peptide inserts into negatively charged microbial membranes, forming pores that cause cell lysis, and demonstrates activity against over 38 bacterial species, 16 fungi, and 16 viruses. Beyond direct antimicrobial effects, LL-37 neutralizes bacterial endotoxin (LPS) by blocking TLR4 signaling, acts as a chemoattractant for immune cells, stimulates angiogenesis, and promotes keratinocyte migration for wound closure. Sensitivity to high salt concentrations and serum proteases limits in vivo half-life, driving research into stabilized analogs and delivery systems. Molecular weight: approximately 4,493.3 Da.
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